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Protein

Basic phospholipase A2 vipoxin B chain

Gene
N/A
Organism
Vipera ammodytes meridionalis (Eastern sand viper)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Heterodimer: postsynaptic neurotoxin.
Monomer: snake venom phospholipase A2 (PLA2) that shows hemolytic activity and inhibition of platelet aggregation. The hemolytic activity occurs only in presence of fatty acids (unsaturated fatty acids facilitate induce a strong hemolytic activity, whereas saturated fatty acids induce a slight activity). The inhibition of platelet aggregation is almost maximal when aggregation is induced by collagen, and arachidonic acid, whereas it is only of 30% when the aggregation is induced by ADP. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.

Catalytic activityi

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.PROSITE-ProRule annotation

Cofactori

Ca2+By similarityNote: Binds 1 Ca2+ ion.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi27 – 271Calcium; via carbonyl oxygenBy similarity
Metal bindingi29 – 291Calcium; via carbonyl oxygenBy similarity
Metal bindingi31 – 311Calcium; via carbonyl oxygenBy similarity
Active sitei47 – 4711 Publication
Metal bindingi48 – 481CalciumBy similarity
Active sitei89 – 8911 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hemostasis impairing toxin, Hydrolase, Neurotoxin, Platelet aggregation inhibiting toxin, Postsynaptic neurotoxin, Toxin

Keywords - Biological processi

Cytolysis, Hemolysis, Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Basic phospholipase A2 vipoxin B chain (EC:3.1.1.4)
Short name:
svPLA2
Alternative name(s):
Phosphatidylcholine 2-acylhydrolase
Vipoxin toxic component
OrganismiVipera ammodytes meridionalis (Eastern sand viper)
Taxonomic identifieri73841 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeViperinaeVipera

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Toxic dosei

LD50 of the heterodimer is 0.7-1.2 mg/kg by intraperitoneal injection into mice and 0.9-1.3 mg/kg by intravenous injection into mice.1 Publication
LD50 of the basic component is 10-13 mg/kg by intraperitoneal injection into mice, and 2.2-3.0 mg/kg by intravenous injection into mice, corresponding to 2.4-fold and more than 10-fold the LD50 of the heterodimer, respectively.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 122122Basic phospholipase A2 vipoxin B chainPRO_0000161712Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi26 ↔ 115Combined sources2 Publications
Disulfide bondi28 ↔ 44Combined sources2 Publications
Disulfide bondi43 ↔ 95Combined sources2 Publications
Disulfide bondi49 ↔ 122Combined sources2 Publications
Disulfide bondi50 ↔ 88Combined sources2 Publications
Disulfide bondi57 ↔ 81Combined sources2 Publications
Disulfide bondi75 ↔ 86Combined sources2 Publications

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Heterodimer of A (AC P04084) and B chains; non-covalently linked. The A chain (acidic) is non-toxic, and increases the toxicity of the B chain (basic). The A chain may act as factor stabilizing the complex structure and hence retaining its toxicity by preventing non-specific binding. Upon binding to the target membranes the A chain is postulated to dissociate.3 Publications

Protein-protein interaction databases

MINTiMINT-220273.

Structurei

Secondary structure

1
122
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 1312Combined sources
Helixi17 – 215Combined sources
Beta strandi22 – 243Combined sources
Turni25 – 273Combined sources
Beta strandi28 – 303Combined sources
Helixi39 – 5214Combined sources
Turni59 – 613Combined sources
Beta strandi66 – 694Combined sources
Beta strandi72 – 754Combined sources
Helixi81 – 9818Combined sources
Helixi100 – 1023Combined sources
Helixi105 – 1073Combined sources
Helixi112 – 1154Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AOKX-ray2.00B1-122[»]
1JLTX-ray1.40B1-122[»]
1RGBX-ray3.30A/B/K/L1-112[»]
ProteinModelPortaliP14420.
SMRiP14420. Positions 1-122.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14420.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG008137.

Family and domain databases

Gene3Di1.20.90.10. 1 hit.
InterProiIPR001211. PLipase_A2.
IPR033112. PLipase_A2_Asp_AS.
IPR016090. PLipase_A2_dom.
IPR033113. PLipase_A2_His_AS.
[Graphical view]
PANTHERiPTHR11716. PTHR11716. 1 hit.
PfamiPF00068. Phospholip_A2_1. 1 hit.
[Graphical view]
PRINTSiPR00389. PHPHLIPASEA2.
SMARTiSM00085. PA2c. 1 hit.
[Graphical view]
SUPFAMiSSF48619. SSF48619. 1 hit.
PROSITEiPS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P14420-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
NLFQFAKMIN GKLGAFSVWN YISYGCYCGW GGQGTPKDAT DRCCFVHDCC
60 70 80 90 100
YGRVRGCNPK LAIYSYSFKK GNIVCGKNNG CLRDICECDR VAANCFHQNK
110 120
NTYNKNYKFL SSSRCRQTSE QC
Length:122
Mass (Da):13,828
Last modified:January 1, 1990 - v1
Checksum:i94438F9F1285FC7D
GO

Sequence databases

PIRiA29290.

Cross-referencesi

Sequence databases

PIRiA29290.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AOKX-ray2.00B1-122[»]
1JLTX-ray1.40B1-122[»]
1RGBX-ray3.30A/B/K/L1-112[»]
ProteinModelPortaliP14420.
SMRiP14420. Positions 1-122.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-220273.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG008137.

Miscellaneous databases

EvolutionaryTraceiP14420.

Family and domain databases

Gene3Di1.20.90.10. 1 hit.
InterProiIPR001211. PLipase_A2.
IPR033112. PLipase_A2_Asp_AS.
IPR016090. PLipase_A2_dom.
IPR033113. PLipase_A2_His_AS.
[Graphical view]
PANTHERiPTHR11716. PTHR11716. 1 hit.
PfamiPF00068. Phospholip_A2_1. 1 hit.
[Graphical view]
PRINTSiPR00389. PHPHLIPASEA2.
SMARTiSM00085. PA2c. 1 hit.
[Graphical view]
SUPFAMiSSF48619. SSF48619. 1 hit.
PROSITEiPS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPA2B_VIPAE
AccessioniPrimary (citable) accession number: P14420
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: May 11, 2016
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The B chain (not complexed with the A chain) does not induce neurotoxic symptoms, hemorrhage, organ injuries and other macroscopic changes.1 Publication

Caution

The acidic chain was originally postulated to act as an inhibitor of the basic chain.Curated

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.